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#32947637   2020/09/18 To Up

Biomarkers and Redox Balance in Aging Rats after Dynamic and Isometric Resistance Training.

Aging muscle is prone to sarcopenia and its associated telomere shortening and increased oxidative stress. Telomeres are protected by a shelterin protein complex, proteins expressed in response to DNA damage. Aerobic exercise training has shown to positively modulate these proteins while aging, but the effects of resistance training are less clear. This investigation was to examine the role of dynamic and isometric RT on markers of senescence and muscle apoptosis: checkpoint kinase 2, 53 kDa protein, shelterin telomere repeat binding 1 and 2, DNA repair, telomere length and redox state in the quadriceps muscle. Fifteen 49-week-old male rats were divided into three groups: control, dynamic resistance training, and isometric resistance training. Dynamic and isometric groups completed five sessions per week during 16 weeks at low to moderate intensity (20-70% maximal load). Only dynamic group decreased expression of 53 kDa protein, proteins from shelterin complex, oxidative stress, and improved antioxidant defense. There was no difference among groups regarding telomere length. In conclusion, dynamic resistance training was more effective than isometric in reducing markers of aging and muscle apoptosis in elderly rats. This modality should be considered as valuable tool do counteract the deleterious effects of aging.
Rodrigo Vanerson Passos Neves, Thiago Dos Santos Rosa, Hugo Luca Corrêa, Kethelen Mariana da Silva Aires, Lysleine Alves Deus, Michel Kendy Sousa, Whitley Jo Stone, Lana Ribeiro Aguiar, Jonato Prestes, Herbert Gustavo Simões, Rosângela Vieira Andrade, Milton Rocha Moraes

1983 related Products with: Biomarkers and Redox Balance in Aging Rats after Dynamic and Isometric Resistance Training.

10 mg 50 UG100 mg100ul200ul25 mg100 mg200 25 MG10 mg100ug

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#32947020   2020/09/15 To Up

Perlecan, a Modular Instructive Proteoglycan with Diverse Functional Properties.

This study reviewed some new aspects of the modular proteoglycan perlecan, a colossal proteoglycan with a 467 kDa core protein and five distinct functional domains. Perlecan is a heparan sulphate proteoglycan that transiently displays native CS sulphation motifs 4-C-3 and 7-D-4 during tissue morphogenesis these are expressed by progenitor cell populations during tissue development. Perlecan is susceptible to fragmentation by proteases during tissue development and in pathological tissues particularly in domains IV and V. The fragmentation pattern of domain IV has been suggested as a means of grading prostate cancer. Domain V of perlecan is of interest due to its interactive properties with integrin α5β1 that promotes pericyte migration enhancing PDGF-BB-induced phosphorylation of PDGFRβ, Src homology region 2 domain-containing phosphatase-2, and focal adhesion kinase supporting the repair of the blood brain barrier following ischaemic stroke. Fragments of domain V can also interact with α2β1 integrin disrupting tube formation by endothelial cells. LG1-LG2, LG3 fragments can antagonise VEGFR2, and α2β1 integrin interactions preventing angiogenesis by endothelial cells. These domain V fragments are of interest as potential anti-tumour agents. Perlecan attached to the luminal surfaces of endothelial cells in blood vessels acts as a flow sensor that signals back to endothelial and smooth muscle cells to regulate vascular tone and blood pressure. Perlecan also acts as a flow sensor in the lacuno-canalicular space regulating osteocytes and bone homeostasis. Along with its biomechanical regulatory properties in cartilaginous tissues this further extends the functional repertoire of this amazingly diverse functional proteoglycan.
James Melrose

1340 related Products with: Perlecan, a Modular Instructive Proteoglycan with Diverse Functional Properties.

1 kit(96 Wells)100ug Lyophilized100ug Lyophilized1 kit(96 Wells)1 ml1 kit(96 Wells)100ug Lyophilized1 kit(96 Wells)40ug/0.2ml100ug Lyophilized100ug Lyophilized1 kit(96 Wells)

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#32946485   2020/09/18 To Up

Transformation of low molecular compounds and soil humic acid by two domain laccase of Streptomyces puniceus in the presence of ferulic and caffeic acids.

The two-domain bacterial laccases oxidize substrates at alkaline pH. The role of natural phenolic compounds in the oxidation of substrates by the enzyme is poorly understood. We have studied the role of ferulic and caffeic acids in the transformation of low molecular weight substrates and of soil humic acid (HA) by two-domain laccase of Streptomyces puniceus (SpSL, previously undescribed). A gene encoding a two-domain laccase was cloned from S. puniceus and over-expressed in Escherichia coli. The recombinant protein was purified by affinity chromatography to an electrophoretically homogeneous state. The enzyme showed high thermal stability, alkaline pH optimum for the oxidation of phenolic substrates and an acidic pH optimum for the oxidation of K4[Fe(CN)6] (potassium ferrocyanide) and ABTS (2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt). Phenolic compounds were oxidized with lower efficiency than K4[Fe(CN)6] and ABTS. The SpSL did not oxidize 3.4-dimethoxybenzoic alcohol and p-hydroxybenzoic acid neither in the absence of phenolic acids nor in their presence. The enzyme polymerized HA-the amount of its high molecular weight fraction (>80 kDa) increased at the expense of low MW fraction (10 kDa). The addition of phenolic acids as potential mediators did not cause the destruction of HA by SpSL. In the absence of the HA, the enzyme polymerized caffeic and ferulic acids to macromolecular fractions (>80 kDa and 10-12 kDa). The interaction of SpSL with HA in the presence of phenolic acids caused an increase in the amount of HA high MW fraction and a two-fold increase in the molecular weight of its low MW fraction (from 10 to 20 kDa), suggesting a cross-coupling reaction. Infrared and solution-state 1H-NMR spectroscopy revealed an increase in the aromaticity of HA after its interaction with phenolic acids. The results of the study expand our knowledge on the transformation of natural substrates by two-domain bacterial laccases and indicate a potentially important role of the enzyme in the formation of soil organic matter (SOM) at alkaline pH values.
Liubov I Trubitsina, Alexander V Lisov, Oxana V Belova, Ivan V Trubitsin, Vladimir V Demin, Andrey I Konstantinov, Anna G Zavarzina, Alexey A Leontievsky

1812 related Products with: Transformation of low molecular compounds and soil humic acid by two domain laccase of Streptomyces puniceus in the presence of ferulic and caffeic acids.

10 mg 5 G200 1000 tests600 Tests / Kit100 ug 1 G500 MG500 mg100ug Lyophilized100 mg

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#32946071   2020/09/18 To Up

Enzymatic degradation of sulphonated azo dye using purified azoreductase from facultative Klebsiella pneumoniae.

Heterologously expressed and purified azoreductase enzyme from facultative Klebsiella pneumoniae was used to degrade sulphonated azo dye. Methyl orange (MO) was used as the model dye to study the azo dye decolorization potential of the purified enzyme at different conditions. The enzyme had maximum activity at 40 °C and pH 8.0. The enzyme was observed to be thermo-stable as some enzyme activity was retained even at 80 °C. The apparent kinetic parameters, i.e., appK and appV, for azoreductase using MO as a substrate were found to be 17.18 μM and 0.08/min, respectively. The purified enzyme was able to decolorize approximately 83% of MO (20 μM) within 10 min in the presence of NADH. Thus, efficient decolorization of MO was observed by the purified enzyme. The recombinant enzyme was purified approximately 18-fold with 46% yield at the end of four steps of the purification process. Enzyme was present in a tetrameric structure as confirmed by the volume at which protein was eluted in gel filtration chromatography, and the monomeric molecular mass of enzyme was found to be 23 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The dye degradation efficiency of azoreductase cloned from Klebsiella pneumoniae and purified from recombinant Escherichia coli was observed to be much higher as compared with the efficiencies of the reported azoreductases from other bacterial strains. In the present study, we report the purification and characterization of the azoreductase cloned from Klebsiella pneumoniae and expressed in Escherichia coli.
Shweta Dixit, Sanjeev Garg

1256 related Products with: Enzymatic degradation of sulphonated azo dye using purified azoreductase from facultative Klebsiella pneumoniae.

1100μl100μl1000mg100μl100μl100μl0.1mg100μl100μl100μl720/kit

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#32944716   2020/09/09 To Up

Comparative study of composition, antioxidant and antimicrobial activity of two adult edible insects from Tenebrionidae family.

In the case of Tenebrionidae family insects, studies focus on larval stage, leaving a lack of information regarding other stages. Therefore, this study was performed in order to understand the differences between the nutritional composition and the bioactivity of two species of this family in their adult stage, fed with a specific diet. Adult beetles of both species were defatted, lyophilized and protein extracted with buffer. Proximal and phytochemical analysis of the extracts of each insect were performed, along with protein extract and hydrolysis analysis by Tris-Tricine and Tris Glycine SDS PAGE. This analysis showed that contained more protein and fat than but contained less crude fiber. The protein extraction was made with PBS, where 130 and 45 kDa bands showed predominant for and less protein was present for . Antioxidant and antimicrobial activities of the enzymatic protein hydrolysates and protein crude extracts were determined. Presence of protein associated with the antioxidant activity were found in both insects. Nonetheless had a higher antioxidant activity with the protein extract in contrast with the higher antioxidant activity shown by once the extracts were digested. After proteolysis, protein extracts showed an increasing antioxidant activity, plus, the ability to inhibit microbial growth of , and . Insect protein hydrolysates with protease open the possibility for the use of these beetles as new sources of encrypted peptides for microbiological control once characterized.
Daniel R Flores, Luz E Casados, Sandra F Velasco, Ana C Ramírez, Gilberto Velázquez

2194 related Products with: Comparative study of composition, antioxidant and antimicrobial activity of two adult edible insects from Tenebrionidae family.

100ug100ug 5 G1 kit100 assays2 x 96 well plate2.5 mg100ug100ul0.05 mg 96 Tests

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#32944709   2019/05/02 To Up

The Influence of Polymer Processing Methods on Polymer Film Physical Properties and Vascular Cell Responsiveness.

Implantable vascular devices typically interface with blood and vascular tissues. Physical properties of device materials and coatings, independent of chemical composition, can significantly influence cell responses and implant success. Here, we analyzed the effect of various polymer processing regimes, using a single implant polymer - poly(ε-caprolactone) (PCL), on vascular endothelial cell (EC), smooth muscle cell (SMC), and platelet response. PCL films were formed by varying three parameters: 1) formation method - solvent casting, melt pressing or spin coating; 2) molecular weight - 50 or 100 kDa; and 3) solvent type - dichloromethane (DCM) or tetrahydrofuran (THF). We quantified the relationship of polymer processing choice to surface roughness, wettability, and bulk stiffness; and to EC adhesion, SMC adhesion, and platelet activity state (PAS). Multiple regression analysis identified which processing method signficantly impacted (F-ratio>p-value; p<0.1) polymer physical properties and vascular cell interaction. Film formation method affected PCL roughness (R), wettability (°), and stiffness (MPa) with spin coating resulting in the most wettable (81.8±0.7°), and stiffest (1.12±0.07 MPa; p<0.001) polymer film; however, solvent cast films were the roughest (281±66nm). Molecular weight influenced wettability, with the highest wettability on 50 kDa films (79.7±0.7°; p<0.001) and DCM solvent films (83.0±1.0°; p<0.01). The multiple regression model confidently predicted (F-ratio=9.88; p=0.005) wettability from molecular weight (p=0.002) and film formation method (p=0.03); stiffness (F-ratio=4.21; p=0.05) also fit well tofilm formation method (p=0.02). Film formation method impacted SMC adhesion and platelet activity state, but not EC adhesion, with melt press PCL promoting the highest SMC adhesion (18000±1536 SMCs; p<0.05) and PAS (5.0±0.7 %PAS). The regression model confidently fit SMC adhesion (F-ratio=3.15; p=0.09) and PAS (F-ratio=5.30; p=0.05) to polymer processing choices, specifically film formation method (p<0.03). However, only SMC adhesion had a model that fit well (F-ratio=4.13; p=0.05) to the physical properties directly, specifically roughness and wettability (p<0.04).
Kaitlyn R Ammann, Maxwell Li, Syed Hossainy, Marvin J Slepian

2146 related Products with: The Influence of Polymer Processing Methods on Polymer Film Physical Properties and Vascular Cell Responsiveness.

100 U100ug Lyophilized250 Units250 Units100ug Lyophilized2500 u500 u100ug Lyophilized20,000 Units 15 ml 250 Units 80 Slides

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#32944148   2020/06/19 To Up

Phylogenetic diversity in and gene clusters between and , as a potential cause of host specificity.

Periodontopathic bacteria in humans and in animals are phylogenetically close and commonly have FimA and Mfa1 fimbriae. However, little is known about how and are phylogenetically different between and . Here, we examined phylogenetic diversity in their and gene clusters.
Kaori Fujiwara-Takahashi, Takayasu Watanabe, Masahiro Shimogishi, Masaki Shibasaki, Makoto Umeda, Yuichi Izumi, Ichiro Nakagawa

1301 related Products with: Phylogenetic diversity in and gene clusters between and , as a potential cause of host specificity.

50 ug 50 ug 50 ug 0.1ml (1mg/ml)200ug96 wells (1 kit)50 ug 96 samples100 plates1 g1mg

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#32944073   2020/09/08 To Up

Recombinant bacteriophage LysKB317 endolysin mitigates infection of corn mash fermentations.

Commercial ethanol fermentation facilities traditionally rely on antibiotics for bacterial contamination control. Here we demonstrate an alternative approach to treat contamination using a novel peptidoglycan hydrolase (LysKB317) isolated from a bacteriophage, EcoSau. This endolysin was specially selected against strains that were isolated as contaminants from a fuel ethanol plant. The LysKB317 gene was recombinantly expressed in as a 33 kDa purified enzyme.
Shao-Yeh Lu, Kenneth M Bischoff, Joseph O Rich, Siqing Liu, Christopher D Skory

1561 related Products with: Recombinant bacteriophage LysKB317 endolysin mitigates infection of corn mash fermentations.

1 mg50 mg10.00 ug1mg5 20.00 ug1001001mg1mg25

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